Speaker
Martin Linden
(Uppsala University, Sweden)
Description
Many proteins and peptides have an intrinsic capacity to
sense and induce membrane curvature, and play crucial roles
for organizing and remodeling cell membranes. However,
neither the molecular driving forces behind these processes
nor the physical models capable of connecting molecular
mechanisms to their large-scale consequences are well
understood. I will describe recent work to develop
computational methods to study these phenomena, and focus on
the relationship between structural symmetry and curvature
sensing.
Structural symmetry is ubiquitous in membrane proteins,
since many of them form symmetric multimeric complexes.
Using coarse-grained simulations and theoretical arguments,
we show that symmetry can greatly influence membrane
curvature sensing. In particular, the potential for
anisotropic membrane curvature sensing is limited to
asymmetric proteins, dimers, and tetramers, but strongly
suppressed by odd and higher-order symmetries. This
classification provides a new perspective on
structure-function relation for membrane proteins, suggests
a correlation between multimer multiplicity and certain
types of membrane deformations, and can simplify the task of
constructing mesoscopic models of curvature sensing.
